2M0Q

Solution NMR analysis of intact KCNE2 in detergent micelles demonstrate a straight transmembrane helix

2M0Q の概要

• エントリーDOI: 10.2210/pdb2m0q/pdb
• NMR情報: BMRB: 18817
• 分子名称: Potassium voltage-gated channel subfamily E member 2 (1 entity in total)
• 機能のキーワード: transmembrane helix, detergent micelle, membrane protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Membrane; Single-pass type I membrane protein: Q9Y6J6
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14486.49

構造登録者

Lai, C.,Li, P.,Chen, L.,Zhang, L.,Wu, F.,Tian, C. (登録日: 2012-11-01, 公開日: 2014-04-30, 最終更新日: 2024-05-15)

主引用文献

Li, P.,Liu, H.,Lai, C.,Sun, P.,Zeng, W.,Wu, F.,Zhang, L.,Wang, S.,Tian, C.,Ding, J.
Differential modulations of KCNQ1 by auxiliary proteins KCNE1 and KCNE2.
Sci Rep, 4:4973-4973, 2014

PubMed Abstract: KCNQ1 channels play vital roles in cardiovascular, gastric and other systems. The conductance and dynamics of KCNQ1 could be modulated by different single transmembrane helical auxiliary proteins (such as KCNE1, KCNE2 and others). In this study, detail KCNQ1 function modulations by different regions of KCNE1 or KCNE2 were examined using combinational methods of electrophysiology, immunofluorescence, solution NMR and related backbone flexibility analysis. In the presence of KCNE2 N-terminus, decreased surface expression and consequent low activities of KCNQ1 were observed. The transmembrane domains (TMDs) of KCNE1 and KCNE2 were illustrated to associate with the KCNQ1 channel in different modes: Ile64 in KCNE2-TMD interacting with Phe340 and Phe275 in KCNQ1, while two pairs of interacting residues (Phe340-Thr58 and Ala244-Tyr65) in the KCNQ1/KCNE1 complex. The KCNE1 C-terminus could modulate gating property of KCNQ1, whereas KCNE2 C-terminus had only minimal influences on KCNQ1. All of the results demonstrated different KCNQ1 function modulations by different regions of the two auxiliary proteins.

PubMed: 24827085
DOI: 10.1038/srep04973

実験手法

SOLUTION NMR